The DOI matches its Crossref record; 128 of the 128 references it cites were found in a registry or an index.
Targeting proteins for degradation.
Open accessAbstract
Protein degradation plays a central role in many cellular functions. Misfolded and damaged proteins are removed from the cell to avoid toxicity. The concentrations of regulatory proteins are adjusted by degradation at the appropriate time. Both foreign and native proteins are digested into small peptides as part of the adaptive immune response. In eukaryotic cells, an ATP-dependent protease called the proteasome is responsible for much of this proteolysis. Proteins are targeted for proteasomal degradation by a two-part degron, which consists of a proteasome binding signal and a degradation initiation site. Here we describe how both components contribute to the specificity of degradation.
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“Because most proteasomal substrates must be ubiquitinated before degradation (Schrader et al., 2009), we next analyzed ubiquitinated proteins in the tibialis anterior muscles by immunoblotting and, as expected, found that their amounts were markedly higher in Rpt3-KO mice than in the Con mice (Figure 4A).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Schrader et al., 2009
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Metadata
- Authors
- Schrader, E. K., Harstad, K. G., & Matouschek, A.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Matouschek, Andreas
- ORCID
- Matouschek, Andreas
- Venue
- Nature Chemical Biology
- Published
- 2009-10-19
- Volume
- 5
- Issue
- 11
- Pages
- 815-822
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC4228941
- OpenAlex
- W4211006098
- Cited by
- 287
- References
- 127
- Citations by year
- 2026: 9 · 2025: 6 · 2024: 14 · 2023: 17 · 2022: 20 · 2021: 15 · 2020: 17 · 2019: 18 · 2018: 14 · 2017: 19 · 2016: 9 · 2015: 10 · 2014: 20 · 2013: 9 · 2012: 25
- FWCI
- 2.27
- Type
- journal article
- Language
- en
- Update notices
- erratum (2009-12-01)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (U54CA143869, T32CA080621)
- National Institute of General Medical Sciences (R01GM64003, R01GM063004, T32GM008061)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- protein degradation, proteasome, proteasomal degradation, degron, ubiquitin ligase, protein targeting, misfolded proteins, adaptive immune response, proteolysis
- MeSH terms
- Valosin Containing Protein, Adenosine Triphosphatases, Adenosine Triphosphate, Bacterial Proteins, Binding Sites, Cell Physiological Phenomena, Ornithine Decarboxylase, Peptide Chain Initiation, Translational, Peptide Hydrolases, Peptides, Proteins, Protein Folding, Cell Cycle Proteins, Ubiquitin, Proteasome Endopeptidase Complex
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